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Uncovering the release mechanism of nucleotide import by HIV-1 capsid
Physical Biology ( IF 2.0 ) Pub Date : 2020-12-01 , DOI: 10.1088/1478-3975/abbf32
Guang Song 1, 2
Affiliation  

Efficient nucleotide import is critical to fuel the reverse DNA synthesis that takes place within the HIV-1 capsid. However, the mechanism by which the HIV-1 capsid imports nucleotides is presently unclear. In this work, we carry out a series of Brownian diffusion simulations to elucidate the nucleotide import process through the hexamer pores of the HIV-1 capsid. Our simulations reveal a significant role of the electrostatic field in the import process and the mechanism by which deoxynucleoside triphosphates (dNTPs) diffuse through the arginine ring: specifically, how IP6s and ATPs, though competing with dNTPs for binding at the pore of the arginine ring, end up accelerating the dNTP import rate by thousands of folds so that it is sufficiently high to fuel the encapsidated DNA synthesis.



中文翻译:

揭示 HIV-1 衣壳输入核苷酸的释放机制

高效的核苷酸输入对于推动 HIV-1 衣壳内发生的反向 DNA 合成至关重要。然而,目前尚不清楚 HIV-1 衣壳输入核苷酸的机制。在这项工作中,我们进行了一系列布朗扩散模拟,以阐明通过 HIV-1 衣壳的六聚体孔的核苷酸输入过程。我们的模拟揭示了静电场在导入过程中的重要作用以及脱氧核苷三磷酸 (dNTPs) 通过精氨酸环扩散的机制:具体而言,IP6 和 ATPs 如何与 dNTPs 竞争结合精氨酸环的孔,最终将 dNTP 导入速度加快了数千倍,因此它足够高,可以为封装的 DNA 合成提供燃料。

更新日期:2020-12-01
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